Lipid Peroxidation and Its Measurement


The oxidative breakdown of polyunsaturated fatty acids in biological membranes, known as lipid peroxidation, refers to a radical-mediated reaction sequence of complex nature. The process is thought to be crucial in the expression of toxicity related to oxidative stress, as membrane integrity is challenged.

Several ways for assessing the occurrence of lipid peroxidation have been developed. Currently, major interest is in the monitoring of lipid peroxidation in intact cells and organs in order to analyze initial stages of oxidative challenge before actual cell death occurs. The introduction of several noninvasive methods has provided advances in this area.

Lipid peroxidation of ω-3 and ω-6 polyunsaturated fatty acids yields ethane and pentane as stable end products, respectively. Thus, intact animals or isolated organs and cells have been analyzed for volatile hydrocarbon evolution.

The reactions of lipid peroxy radicals according to Russell’s mechanism generate singlet molecular oxygen which, in turn, may generate low-level chemiluminescence in the near-infrared. Using sensitive detection methods for these photoemissive species, studies with intact organs and cells have shown good correlation of low-level chemiluminescence with other parameters of lipid peroxidation.

Regarding invasive methods, conjugated dienes and malondialdehyde have been used in numerous studies for the detection of lipid peroxidation. Other products of interest include the assay of lipid peroxides, lipid aldehydes, lipid expoxides, and subsequent products such as fluorescent compounds that may form with cellular constituents.


Lipid Peroxidation Lipid Hydroperoxide Peroxy Radical Glutathione Transferase Actual Cell Death 
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  1. 1.
    Sies, H., ed. “Oxidative Stress.” Academic Press, London, 1985.Google Scholar
  2. 2.
    Kappus, H. Lipid peroxidation: Mechanisms, analysis, enzymology and biological relevance. In: Ref. 1, pp. 273–310.Google Scholar
  3. 3.
    Packer, L., ed. “Oxygen Radicals in Biological Systems. Methods in Enzymology,” Vol. 105. Academic Press, Orlando, 1984.Google Scholar
  4. 4.
    Slater, T. F. Overview of methods used for detecting lipid peroxidation. In: Ref. 3, pp. 283–293.Google Scholar
  5. 5.
    Riely, C. A., Cohen, G., and Lieberman, M. Ethane evolution: A new index of lipid peroxidation. Science 183: 208–210, 1974.PubMedCrossRefGoogle Scholar
  6. 6.
    Lawrence, G. D., and Cohen, G. Concentrating ethane from breath to monitor lipid peroxidation in vivo. In: Ref. 3, pp. 305–311.Google Scholar
  7. 7.
    Müller, A., and Sies, H. Assay of ethane and pentane from isolated organs and cells. In: Ref. 3, pp. 311–319.Google Scholar
  8. 8.
    Frank, H., Hintze, T., Bimboes, D., and Remmer, H. Monitoring lipid peroxydation by breath analysis: Endogenous hydrocarbons and their metabolic elimination. Toxicol. Appl. Pharmacol. 56: 337–344, 1980.PubMedCrossRefGoogle Scholar
  9. 9.
    Cadenas, E., and Sies, H. Low-level chemiluminescence as an indicator of singlet molecular oxygen in biological systems. In: Ref. 3, pp. 221–231.Google Scholar
  10. 10.
    Boveris, A., Cadenas, E., Reiter, R., Filipkowski, M., Nakase, Y., and Chance, B. Organ chemiluminescence: Noninvasive assay for oxidative radical reactions. Proc. Natl. Acad. Sci. USA 77: 347–351, 1979.CrossRefGoogle Scholar
  11. 11.
    Sies, H., and Cadenas, E. Oxidative stress: Damage to intact cells and organs. Philos. Trans. R. Soc. Lond. (Biol.) 311: 617–631, 1985.CrossRefGoogle Scholar
  12. 12.
    Cilento, G. Electronic excitation in dark biological processes. In: “Chemical and Biological Generation of Excited States.” W. Adam and G. Cilento, eds. Academic Press, New York, 1982, pp. 277–307.Google Scholar
  13. 13.
    Russell, G. A. Deuterium-isotope effects in the autoxidation of aralkyl hydrocarbons. Mechanism of interaction of peroxy radicals. J. Am. Chem. Soc. 79: 3871–3877, 1957.CrossRefGoogle Scholar
  14. 14.
    Howard, J. A., and Ingold, K. U. Rate constants for self-reactions of n-and t-butyl peroxy radicals and cyclohexylperoxy radicals. The deuterium isotope effects in the termination of secondary peroxy radicals. J. Am. Chem. Soc. 90: 1058–1059, 1968.CrossRefGoogle Scholar
  15. 15.
    De Luzio, N. R., and Stege, T. E. Enhanced hepatic chemiluminescence following carbon tetrachloride or hydrazine administration. Life Sci. 21: 1457–1464, 1977.PubMedCrossRefGoogle Scholar
  16. 16.
    Cadenas, E., Varsavsky, A. I., Boveris, A., and Chance, B. Oxygen-or organic hydroperoxide-induced chemiluminescence of brain and liver homogenates. Biochem. J. 198: 645–654, 1981.PubMedGoogle Scholar
  17. 17.
    Cadenas, E., Wefers, H., and Sies, H. Low level chemiluminescence of isolated hepatocytes. Eur. J. Biochem. 119: 531–536, 1981.PubMedCrossRefGoogle Scholar
  18. 18.
    Sugioka, K., and Nakano, M. A possible mechanism of the generation of singlet oxygen in NADPH-dependent microsomal lipoperoxidation. Biochim. Biophys. Acta 423: 203–216, 1976.PubMedCrossRefGoogle Scholar
  19. 19.
    Noll, T., de Groot, H., and Sies, H. Distinct temporal relation between oxygen uptake, malondialdehyde formation and low-level chemiluminescence during microsomal lipid peroxidation. Arch. Biochem. Biophys., in press.Google Scholar
  20. 20.
    Aust, S. D. Lipid peroxidation. In: “Handbook of Methods for Oxygen Radical Research.” R. A. Greenwald, ed. CRC Press, Boca Raton, 1985, pp. 203–207.Google Scholar
  21. 21.
    Bird, R. P., and Draper, H. H. Comparative studies on different methods of malonaldehyde determination. In: Ref. 3, pp. 299–305.Google Scholar
  22. 22.
    Esterbauer, H., Lang, J., Zadravec, S., and Slater, T. F. Detection of malonaldehyde by high-performance liquid chromatography. In: Ref. 3, pp. 319–328.Google Scholar
  23. 23.
    Pryor, W. A., and Castle, L. Chemical methods for the detection of lipid hydroperoxides. In: Ref. 3, pp. 293–299.Google Scholar
  24. 24.
    Cathcart, R., Schwiers, E., and Ames, B. N. Detection of picomole levels of lipid hydroperoxides using a dichlorofluorescin fluorescent assay. In: Ref. 3, pp. 352–358.Google Scholar
  25. 25.
    Marshall, P. J., Warso, M. A., and Lands, W. E. M. Selective microdetermination of lipid hydroperoxides. Anal. Biochem. 145: 192–199, 1985.PubMedCrossRefGoogle Scholar
  26. 26.
    Yamamoto, Y., Brodsky, M. H., Baker, J. C., and Ames, B. N. Detection and characterization of lipid hydroperoxides at picomole levels by high performance liquid chromatography. Anal. Biochem., in press.Google Scholar
  27. 27.
    Recknagel, R. O., and Glende, E. A., Jr. Spectrophotometric detection of lipid conjugated dienes. In: Ref. 3, pp. 331–337.Google Scholar
  28. 28.
    Dillard, C. J., and Tappel, A. L. Fluorescent damage products of lipid peroxidation. In: Ref. 3, pp. 337–341.Google Scholar
  29. 29.
    Stark, W. S., Miller, G. V., and Itoku, K. A. Calibration of microphotometers as it applies to the detection of lipofuscin and the blue-and yellow-emitting fluorophores in situ. In: Ref. 3, pp. 341–347.Google Scholar
  30. 30.
    Comporti, M. Biology of disease. Lipid peroxidation and cellular damage in toxic liver injury. Lab. Invest. 53: 599–623, 1985.PubMedGoogle Scholar
  31. 31.
    Benedetti, A., Casini, A. F., Ferrali, M., and Comporti, M. Effects of diffusible products of peroxidation of rat liver microsomal lipids. Biochem. J. 180: 303–312, 1979.PubMedGoogle Scholar
  32. 32.
    Fogelman, M. A., Shechter, I., Seager, J., Hokom, M., Child, J. S., and Edwards, P. A. Malondialdehyde alteration of low density lipoproteins leads to cholesteryl ester accumulation in human monocyte-macrophages. Proc. Natl. Acad. Sci. USA 77: 2214–2218, 1980.PubMedCrossRefGoogle Scholar
  33. 33.
    Jürgens, G., Lang, J., and Esterbauer, H. Modification of human low-density lipoprotein by the lipid peroxidation product 4-hydroxynonenal. Biochim. Biophys. Acta 875: 103–114, 1986.PubMedGoogle Scholar
  34. 34.
    Alin, P., Danielson, U. H., and Mannervik, B. 4-Hydroxyalk-2-enals are substrates for glutathione transferase. FEBS Lett. 179: 267–270, 1985.PubMedCrossRefGoogle Scholar
  35. 35.
    Ishikawa, T., Esterbauer, H., and Sies, H. Role of cardiac glutathione transferase and of the glutathione S-conjugate export system in biotransformation of 4-hydroxynonenal in the heart. J. Biol. Chem. 261: 1576–1581, 1986.PubMedGoogle Scholar
  36. 36.
    Jenssen, H., Guthenberg, C., Alin, P., and Mannervik, B. Rat glutathione transferase 8-8, an enzyme efficiently detoxifying 4-hydroxyalk-2-enals. FEBS Lett. 203: 207–209, 1986.CrossRefGoogle Scholar
  37. 37.
    Ishikawa, T., Zimmer, M., and Sies, H. Energy-linked cardiac transport system for glutathione disulfide. FEBS Lett. 200: 128–132, 1986.PubMedCrossRefGoogle Scholar

Copyright information

© Plenum Press, New York 1987

Authors and Affiliations

  • H. Sies
    • 1
  1. 1.Institut für Physiologische ChemieUniversität DüsseldorfDüsseldorfWest Germany

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